The C-terminal region of translesion synthesis DNA polymerase η is partially unstructured and has high conformational flexibility.

ABSTRACT: Eukaryotic DNA polymerase η catalyzes translesion synthesis of thymine dimers and 8-oxoguanines. It is comprised of a polymerase domain and a C-terminal region, both of which are required for its biological function. The C-terminal region mediates interactions with proliferating cell nuclear antigen (PCNA) and other translesion synthesis proteins such as Rev1. This region contains a ubiquitin-binding/zinc-binding (UBZ) motif and a PCNA-interacting protein (PIP) motif. Currently little structural information is available for this region of polymerase η. Using a combination of approaches-including genetic complementation assays, X-ray crystallography, Langevin dynamics simulations, and small-angle X-ray scattering-we show that the C-terminal region is partially unstructured and has high conf

SUBMITTER: Powers KT 

PROVIDER: S-EPMC5829636 | biostudies-literature | 2018 Feb

REPOSITORIES: biostudies-literature